open access

https://hdl.handle.net/2115/67501

Biochemical Characterization of a Thermophilic Cellobiose 2-Epimerase from a Thermohalophilic Bacterium,Rhodothermus marinusJCM9785

英語

N-acetylglucosamine 2-epimerase

2011-11

Taylor & Francis

Bioscience, Biotechnology, and Biochemistry

75(11)

2162-2168

Cellobiose 2-epimerase (CE) reversibly converts glucose residue to mannose residue at the reducing end of β-1,4-linked oligosaccharides. It efficiently produces epilactose carrying prebiotic properties from lactose, but the utilization of known CEs is limited due to thermolability. We focused on thermoholophilic Rhodothermus marinus JCM9785 as a CE producer, since a CE-like gene was found in the genome of R. marinus DSM4252. CE activity was detected in the cell extract of R. marinus JCM9785. The deduced amino acid sequence of the CE gene from R. marinus JCM9785 (RmCE) was 94.2% identical to that from R. marinus DSM4252. The N-terminal amino acid sequence and tryptic peptide masses of the native enzyme matched those of RmCE. The recombinant RmCE was most active at 80 °C at pH 6.3, and stable in a range of pH 3.2–10.8 and below 80 °C. In contrast to other CEs, RmCE demonstrated higher preference for lactose over cellobiose.

学術雑誌論文

Accepted Manuscript

This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience biotechnology and biochemistry on 11/2011, available online: http://wwww.tandfonline.com/10.1271/bbb.110456

0916-8451

1347-6947

AA10824164